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Description

Overview

A 22-amino acid PDZ domain-binding carboxamide toward Dvl (dishevelled) family proteins is fused at the N-terminal with a 16-mer antennapedia homeodomain-derived cell-permeable acetamide to facilitate its use in cellular studies. Shown to selectively inhibit the upregulation of cellular β-catenin accumulation and transcription activity upon Wnt3a stimulation (IC50 = 11 µM) or Dvl1/2/3 overexpression in HEK293 cultures, but not the Wnt3a- or Dvl1/2/3-independent, constitutively active Wnt pathway signaling in the APC-mutant HCT-15 colon cancer cells. Unlike Box5, the PDZ-interacting sequence in Pen-N3, originally identified via a random phage display screening, is not derived from Wnt or other known cellular proteins.

Documentation

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Certificates of Analysis

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Lot Number

322337

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References

Reference overview

Zhang, Y., et al. 2009. Nat. Chem. Biol.5, 217.

Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

A 22-amino acid PDZ domain-binding carboxamide toward Dvl (dishevelled) family proteins is fused at the N-terminal with a 16-mer antennapedia homeodomain-derived cell-permeable acetamide to facilitate its use in cellular studies. Shown to selectively inhibit the upregulation of cellular β-catenin accumulation and transcription activity upon Wnt3a stimulation (IC50 = 11 µM) or Dvl1/2/3 overexpression in HEK293 cultures, but not the Wnt3a- or Dvl1/2/3-independent, constitutively active Wnt pathway signaling in the APC-mutant HCT-15 colon cancer cells. Unlike Box5, the PDZ-interacting sequence in Pen-N3, originally identified via a random phage display screening, is not derived from Wnt or other known cellular proteins.